Evidence map›Paper›PMID 25542993›Full record

ReviewProgress in biophysics and molecular biology2015

Characteristics and concepts of dynamic hub proteins in DNA processing machinery from studies of RPA.

Norie Sugitani, Walter J Chazin

Abstract readReview
In one paragraph

Review in Progress in biophysics and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017
    Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Norie SugitaniCenter for Structural Biology and Departments of Biochemistry and Chemistry, Vanderbilt University, Nashville, TN, USA.
Walter J ChazinCenter for Structural Biology and Departments of Biochemistry and Chemistry, Vanderbilt University, Nashville, TN, USA. Electronic address: Walter.chazin@vanderbilt.edu.

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Structural Basis for RPA Functions in DNA ProcessingR01GM065484 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2003 to 2015
$3.9M
Synthesis, StructUre and Replication of Carcirogen-Modified OligonucleotidesR01ES016561 · NIEHS · VANDERBILT UNIVERSITY · PI RIZZO, CARMELO J · 2010 to 2014
$1.7M
NCI NIH HHS P01 CA092584NCI NIH HHS P30 CA068485NIEHS NIH HHS P30 ES000267NIEHS NIH HHS P30 ES00267NIEHS NIH HHS R01 ES016561NIGMS NIH HHS R01 GM065484NIGMS NIH HHS R01 GM65484NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

DNA replication, damage response and repair require the coordinated action of multi-domain proteins operating within dynamic multi-protein machines that act upon the DNA substrate. These modular proteins contain flexible linkers of various lengths, which enable changes in the spatial distribution of the globular domains (architecture) that harbor their essential biochemical functions. This mobile architecture is uniquely suited to follow the evolving substrate landscape present over the course of the specific process performed by the multi-protein machinery. A fundamental advance in understanding of protein machinery is the realization of the pervasive role of dynamics. Not only is the machine undergoing dynamic transformations, but the proteins themselves are flexible and constantly adapting to the progression through the steps of the overall process. Within this dynamic context the activity of the constituent proteins must be coordinated, a role typically played by hub proteins. A number of important characteristics of modular proteins and concepts about the operation of dynamic machinery have been discerned. These provide the underlying basis for the action of the machinery that reads DNA, and responds to and repairs DNA damage. Here, we introduce a number of key characteristics and concepts, including the modularity of the proteins, linkage of weak binding sites, direct competition between sites, and allostery, using the well recognized hub protein replication protein A (RPA).

Indexed as

AnimalsBinding SitesDNADNA DamageDNA RepairDNA ReplicationHumansModels, ChemicalModels, GeneticModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationReplication Protein ADNAReplication Protein AAllosteryDNA mimicryDNA repairDNA replicationMultivalent interactionsReplication protein A

Identifiers

PMID25542993
PMCPMC4417437

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.